Biochemical analysis of the extracellular matrix in the bovine periodontal ligament

Abstract

In order to study the function of the extracellular matrix (ECM) in the bovine periodontal ligament, I carried out biochemical investigations of the collagen and glycosaminoglycans in this tissue from 6 mandibular anterior teeth (APL) and 6 maxillary posterior teeth (PPL). The GAG from both locations consisted of the same 4 molecules: dermatan sulfate (DS), chondroitin sulfate, hyaluronic acid, and heparin sulfate. However, there was significantly more DS in the APL than in the PPL. Investigation of the unsaturated disaccharide component of DS revealed significantly more ΔDi-4S from the DS in the APL than in the PPL. Also, there was significantly more collagen (hydroxyproline) in the APL, although the chemical composition for this component was the same for both regions. These results indicate that the APL has a stronger tendency than the PPL to form fibers, and that metabolism in the ECM changes in response to the support function of the periodontal ligament.